title: Beta-conglycinin embeds active peptides that inhibit lipid accumulation in 3T3-L1 adipocytes in vitro.
abstract: Obesity is a worldwide health concern because it is a well-recognized predictor of premature mortality. The objective was to identify soybean varieties that have improved potential to inhibit fat accumulation in adipocytes by testing the effects of soy hydrolysates having a range of protein subunit compositions on lipid accumulation and adiponectin expression in 3T3-L1 adipocytes. The results showed that differences in the protein distribution of 15 soy genotypes led to different potentials for the reduction of fat accumulation. The inhibition of lipid accumulation of soy alcalase hydrolysates in 3T3-L1 adipocytes ranged from 29 to 46%. Soy hydrolysates made from genotypes with 45.3 +/- 3.3% of total protein as beta-conglycinin, on average, showed significantly higher inhibition of lipid accumulation compared to those with 24.7 +/- 1.5% of extracted total protein as beta-conglycinin. Moreover, after in vitro simulated digestion with pepsin-pancreatin of the soy alcalase hydrolysates, 86% of the original activity remained. Adiponectin expression was induced in 3T3-L1 adipocytes treated with 15 soy hydrolysates up to 2.49- and 2.63-fold for high and low molecular weight adiponectin, respectively. The inhibition of lipid accumulation calculated from a partial least squares (PLS) analysis model correlated well with experimental data (R(2) = 0.91). In conclusion, it was feasible to differentiate soy varieties on the basis of the potential of their proteins to reduce fat accumulation using a statistical model and a cell-based assay in vitro. Furthermore, beta-conglycinin embeds more peptides than glycinin subunits that inhibit lipid accumulation and induce adiponectin in 3T3-L1 adipocytes. Therefore, soy ingredients containing beta-conglycinin may be important food components for the control of lipid accumulation in adipose tissue.
authors.affiliation: Department of Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, Illinois 61801, USA.
authors.forename: Cristina
authors.initials: C
authors.lastname: Martinez-Villaluenga
authors.forename: Neal A
authors.initials: NA
authors.lastname: Bringe
authors.forename: Mark A
authors.initials: MA
authors.lastname: Berhow
authors.forename: Elvira
authors.initials: E
authors.lastname: Gonzalez de Mejia
mesh_terms: D041721:3T3-L1 Cells; D017667:Adipocytes / Q000187:drug effects / Q000378:metabolism*; D052242:Adiponectin / Q000096:biosynthesis; D000818:Animals; D052179:Antigens, Plant; D005838:Genotype; D005916:Globulins / Q000032:analysis / Q000737:chemistry* / Q000494:pharmacology*; D006868:Hydrolysis; D050356:Lipid Metabolism / Q000187:drug effects*; D051379:Mice; D055314:Seed Storage Proteins / Q000032:analysis / Q000737:chemistry* / Q000494:pharmacology*; D030262:Soybean Proteins / Q000032:analysis / Q000737:chemistry* / Q000494:pharmacology*; D013025:Glycine max / Q000737:chemistry / Q000235:genetics; D013381:Subtilisins / Q000378:metabolism
chemical_list: D052242:Adiponectin; D052179:Antigens, Plant; D005916:Globulins; D055314:Seed Storage Proteins; D030262:Soybean Proteins; C013894:beta-conglycinin protein, Glycine max; C011474:glycinin; D013381:Subtilisins